MED20_HUMAN
ID MED20_HUMAN Reviewed; 212 AA.
AC Q9H944; B4DE08; O95821; Q5T8J4; Q9Y429;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Mediator of RNA polymerase II transcription subunit 20;
DE AltName: Full=Mediator complex subunit 20;
DE AltName: Full=TRF-proximal protein homolog;
DE Short=hTRFP;
GN Name=MED20; Synonyms=TRFP;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PROTEIN SEQUENCE OF 16-26; 36-51
RP AND 205-212, AND INTERACTION WITH RNA POLYMERASE II AND MED21.
RX PubMed=9933582; DOI=10.1074/jbc.274.7.3937;
RA Xiao H., Tao Y., Roeder R.G.;
RT "The human homologue of Drosophila TRF-proximal protein is associated with
RT an RNA polymerase II-SRB complex.";
RL J. Biol. Chem. 274:3937-3940(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Liver, Prostate, Testis, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 120-212 (ISOFORM 1).
RC TISSUE=Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP INTERACTION WITH MED18.
RX PubMed=12584197; DOI=10.1074/jbc.c300054200;
RA Sato S., Tomomori-Sato C., Banks C.A.S., Sorokina I., Parmely T.J.,
RA Kong S.E., Jin J., Cai Y., Lane W.S., Brower C.S., Conaway R.C.,
RA Conaway J.W.;
RT "Identification of mammalian Mediator subunits with similarities to yeast
RT Mediator subunits Srb5, Srb6, Med11, and Rox3.";
RL J. Biol. Chem. 278:15123-15127(2003).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE MEDIATOR
RP COMPLEX.
RX PubMed=15175163; DOI=10.1016/j.molcel.2004.05.006;
RA Sato S., Tomomori-Sato C., Parmely T.J., Florens L., Zybailov B.,
RA Swanson S.K., Banks C.A.S., Jin J., Cai Y., Washburn M.P., Conaway J.W.,
RA Conaway R.C.;
RT "A set of consensus mammalian mediator subunits identified by
RT multidimensional protein identification technology.";
RL Mol. Cell 14:685-691(2004).
RN [8]
RP INTERACTION WITH MED1; MED18; MED21; MED28; MED29 AND MED31, IDENTIFICATION
RP BY MASS SPECTROMETRY, IDENTIFICATION IN THE MEDIATOR COMPLEX, AND
RP ASSOCIATION OF THE MEDIATOR COMPLEX WITH RNA POLYMERASE II.
RX PubMed=15989967; DOI=10.1016/j.molcel.2005.05.015;
RA Zhang X., Krutchinsky A., Fukuda A., Chen W., Yamamura S., Chait B.T.,
RA Roeder R.G.;
RT "MED1/TRAP220 exists predominantly in a TRAP/Mediator subpopulation
RT enriched in RNA polymerase II and is required for ER-mediated
RT transcription.";
RL Mol. Cell 19:89-100(2005).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Component of the Mediator complex, a coactivator involved in
CC the regulated transcription of nearly all RNA polymerase II-dependent
CC genes. Mediator functions as a bridge to convey information from gene-
CC specific regulatory proteins to the basal RNA polymerase II
CC transcription machinery. Mediator is recruited to promoters by direct
CC interactions with regulatory proteins and serves as a scaffold for the
CC assembly of a functional preinitiation complex with RNA polymerase II
CC and the general transcription factors.
CC -!- SUBUNIT: Interacts with PPARG (By similarity). Component of the
CC Mediator complex, which is composed of MED1, MED4, MED6, MED7, MED8,
CC MED9, MED10, MED11, MED12, MED13, MED13L, MED14, MED15, MED16, MED17,
CC MED18, MED19, MED20, MED21, MED22, MED23, MED24, MED25, MED26, MED27,
CC MED29, MED30, MED31, CCNC, CDK8 and CDC2L6/CDK11. The MED12, MED13,
CC CCNC and CDK8 subunits form a distinct module termed the CDK8 module.
CC Mediator containing the CDK8 module is less active than Mediator
CC lacking this module in supporting transcriptional activation.
CC Individual preparations of the Mediator complex lacking one or more
CC distinct subunits have been variously termed ARC, CRSP, DRIP, PC2, SMCC
CC and TRAP. {ECO:0000250, ECO:0000269|PubMed:12584197,
CC ECO:0000269|PubMed:15175163, ECO:0000269|PubMed:15989967,
CC ECO:0000269|PubMed:9933582}.
CC -!- INTERACTION:
CC Q9H944; Q49AR9: ANKS1A; NbExp=3; IntAct=EBI-394644, EBI-11954519;
CC Q9H944; Q6BCY4-2: CYB5R2; NbExp=3; IntAct=EBI-394644, EBI-12102608;
CC Q9H944; Q96DN0: ERP27; NbExp=3; IntAct=EBI-394644, EBI-953772;
CC Q9H944; Q06547: GABPB1; NbExp=3; IntAct=EBI-394644, EBI-618165;
CC Q9H944; Q6IPE9: MARK4; NbExp=3; IntAct=EBI-394644, EBI-10250211;
CC Q9H944; Q9BUE0: MED18; NbExp=21; IntAct=EBI-394644, EBI-394640;
CC Q9H944; Q9NX70: MED29; NbExp=6; IntAct=EBI-394644, EBI-394656;
CC Q9H944; Q8WWB5: PIH1D2; NbExp=3; IntAct=EBI-394644, EBI-10232538;
CC Q9H944; Q9UIG4: PSORS1C2; NbExp=3; IntAct=EBI-394644, EBI-11974061;
CC Q9H944; Q6ZRS2-3: SRCAP; NbExp=3; IntAct=EBI-394644, EBI-12029182;
CC Q9H944; Q86WT6-2: TRIM69; NbExp=3; IntAct=EBI-394644, EBI-11525489;
CC Q9H944; P25490: YY1; NbExp=3; IntAct=EBI-394644, EBI-765538;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H944-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H944-2; Sequence=VSP_057052;
CC -!- SIMILARITY: Belongs to the Mediator complex subunit 20 family.
CC {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF097725; AAD16169.1; -; mRNA.
DR EMBL; AK023092; BAB14399.1; -; mRNA.
DR EMBL; AK293412; BAG56919.1; -; mRNA.
DR EMBL; AL160163; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC012618; AAH12618.1; -; mRNA.
DR EMBL; BC019866; AAH19866.1; -; mRNA.
DR EMBL; BC032552; AAH32552.1; -; mRNA.
DR EMBL; BC040950; AAH40950.1; -; mRNA.
DR EMBL; AL050196; CAB43314.1; -; mRNA.
DR CCDS; CCDS4862.1; -. [Q9H944-1]
DR CCDS; CCDS83085.1; -. [Q9H944-2]
DR PIR; T08801; T08801.
DR RefSeq; NP_001292384.1; NM_001305455.1.
DR RefSeq; NP_001292385.1; NM_001305456.1.
DR RefSeq; NP_001292386.1; NM_001305457.1. [Q9H944-2]
DR RefSeq; NP_004266.2; NM_004275.4. [Q9H944-1]
DR PDB; 7EMF; EM; 3.50 A; T=1-212.
DR PDB; 7ENA; EM; 4.07 A; t=1-212.
DR PDB; 7ENC; EM; 4.13 A; t=1-212.
DR PDB; 7ENJ; EM; 4.40 A; T=1-212.
DR PDB; 7LBM; EM; 4.80 A; l=1-212.
DR PDB; 7NVR; EM; 4.50 A; f=1-212.
DR PDBsum; 7EMF; -.
DR PDBsum; 7ENA; -.
DR PDBsum; 7ENC; -.
DR PDBsum; 7ENJ; -.
DR PDBsum; 7LBM; -.
DR PDBsum; 7NVR; -.
DR AlphaFoldDB; Q9H944; -.
DR SMR; Q9H944; -.
DR BioGRID; 114862; 173.
DR ComplexPortal; CPX-3227; Core mediator complex.
DR CORUM; Q9H944; -.
DR DIP; DIP-31449N; -.
DR IntAct; Q9H944; 137.
DR MINT; Q9H944; -.
DR STRING; 9606.ENSP00000265350; -.
DR GlyGen; Q9H944; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9H944; -.
DR MetOSite; Q9H944; -.
DR PhosphoSitePlus; Q9H944; -.
DR SwissPalm; Q9H944; -.
DR BioMuta; MED20; -.
DR DMDM; 29428258; -.
DR EPD; Q9H944; -.
DR jPOST; Q9H944; -.
DR MassIVE; Q9H944; -.
DR MaxQB; Q9H944; -.
DR PaxDb; Q9H944; -.
DR PeptideAtlas; Q9H944; -.
DR PRIDE; Q9H944; -.
DR ProteomicsDB; 3912; -.
DR ProteomicsDB; 81283; -. [Q9H944-1]
DR TopDownProteomics; Q9H944-1; -. [Q9H944-1]
DR Antibodypedia; 30105; 106 antibodies from 24 providers.
DR DNASU; 9477; -.
DR Ensembl; ENST00000265350.9; ENSP00000265350.4; ENSG00000124641.16. [Q9H944-1]
DR Ensembl; ENST00000409312.5; ENSP00000386816.1; ENSG00000124641.16. [Q9H944-2]
DR GeneID; 9477; -.
DR KEGG; hsa:9477; -.
DR MANE-Select; ENST00000265350.9; ENSP00000265350.4; NM_004275.5; NP_004266.2.
DR UCSC; uc003ork.4; human. [Q9H944-1]
DR CTD; 9477; -.
DR DisGeNET; 9477; -.
DR GeneCards; MED20; -.
DR HGNC; HGNC:16840; MED20.
DR HPA; ENSG00000124641; Low tissue specificity.
DR MIM; 612915; gene.
DR neXtProt; NX_Q9H944; -.
DR OpenTargets; ENSG00000124641; -.
DR PharmGKB; PA162395472; -.
DR VEuPathDB; HostDB:ENSG00000124641; -.
DR eggNOG; KOG4309; Eukaryota.
DR GeneTree; ENSGT00390000002060; -.
DR HOGENOM; CLU_080044_1_0_1; -.
DR InParanoid; Q9H944; -.
DR OMA; QSTFSIC; -.
DR OrthoDB; 1112080at2759; -.
DR PhylomeDB; Q9H944; -.
DR TreeFam; TF315156; -.
DR PathwayCommons; Q9H944; -.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-212436; Generic Transcription Pathway.
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR SignaLink; Q9H944; -.
DR SIGNOR; Q9H944; -.
DR BioGRID-ORCS; 9477; 652 hits in 1032 CRISPR screens.
DR ChiTaRS; MED20; human.
DR GenomeRNAi; 9477; -.
DR Pharos; Q9H944; Tbio.
DR PRO; PR:Q9H944; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q9H944; protein.
DR Bgee; ENSG00000124641; Expressed in secondary oocyte and 168 other tissues.
DR ExpressionAtlas; Q9H944; baseline and differential.
DR Genevisible; Q9H944; HS.
DR GO; GO:0070847; C:core mediator complex; IPI:ComplexPortal.
DR GO; GO:0016592; C:mediator complex; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:ComplexPortal.
DR GO; GO:0003899; F:DNA-directed 5'-3' RNA polymerase activity; NAS:UniProtKB.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0032968; P:positive regulation of transcription elongation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0060261; P:positive regulation of transcription initiation from RNA polymerase II promoter; IC:ComplexPortal.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0051123; P:RNA polymerase II preinitiation complex assembly; IC:ComplexPortal.
DR GO; GO:0035914; P:skeletal muscle cell differentiation; IEA:Ensembl.
DR GO; GO:0006366; P:transcription by RNA polymerase II; TAS:ProtInc.
DR GO; GO:0006351; P:transcription, DNA-templated; NAS:UniProtKB.
DR InterPro; IPR013921; Mediator_Med20.
DR PANTHER; PTHR12465; PTHR12465; 1.
DR Pfam; PF08612; Med20; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Activator; Alternative splicing; Direct protein sequencing;
KW Nucleus; Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..212
FT /note="Mediator of RNA polymerase II transcription subunit
FT 20"
FT /id="PRO_0000065731"
FT VAR_SEQ 117..212
FT /note="YQYCDFLVKVGTVTMGPSARGISVEVEYGPCVVASDCWSLLLEFLQSFLGSH
FT TPGAPAVFGNRHDAVYGPADTMVQYMELFNKIRKQQQVPVAGIR -> WSMAPVW (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057052"
FT CONFLICT 134..136
FT /note="SAR -> VP (in Ref. 1; AAD16169)"
FT /evidence="ECO:0000305"
FT CONFLICT 206..207
FT /note="Missing (in Ref. 1; AAD16169)"
FT /evidence="ECO:0000305"
FT STRAND 3..9
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 34..47
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 62..67
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 69..71
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 74..82
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 84..88
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 91..98
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 110..131
FT /evidence="ECO:0007829|PDB:7EMF"
FT STRAND 134..146
FT /evidence="ECO:0007829|PDB:7EMF"
FT TURN 150..152
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:7EMF"
FT HELIX 186..203
FT /evidence="ECO:0007829|PDB:7EMF"
SQ SEQUENCE 212 AA; 23222 MW; 5AA7A39981EB1498 CRC64;
MGVTCVSQMP VAEGKSVQQT VELLTRKLEM LGAEKQGTFC VDCETYHTAA STLGSQGQTG
KLMYVMHNSE YPLSCFALFE NGPCLIADTN FDVLMVKLKG FFQSAKASKI ETRGTRYQYC
DFLVKVGTVT MGPSARGISV EVEYGPCVVA SDCWSLLLEF LQSFLGSHTP GAPAVFGNRH
DAVYGPADTM VQYMELFNKI RKQQQVPVAG IR
